Export your current network:
... as a vector graphic:
SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc
... as short tabular text output:
TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)
... as tabular text output:
TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)
... as an XML summary:
structured XML interaction data, according to the 'PSI-MI' data standard
... protein node degrees:
node degree of proteins in your network (given the current score cut-off)
... network coordinates:
a flat-file format describing the coordinates and colors of nodes in the network
... protein sequences:
MFA: multi-fasta format - containing the aminoacid sequences in the network
... protein annotations:
a tab-delimited file describing the names, domains and descriptions of proteins in your network
... functional annotations:
a tab-delimited file containing all known functional terms of proteins in your network
Browse interactions in tabular form:
| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| FAD_0293 | dnaJ | FAD_0293 | FAD_0534 | Tetratricopeptide repeat-containing protein. | Chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and [...] | 0.714 |
| FAD_0293 | dnaK | FAD_0293 | FAD_0533 | Tetratricopeptide repeat-containing protein. | Chaperone DnaK; Acts as a chaperone. | 0.728 |
| FAD_0293 | hscA | FAD_0293 | FAD_0761 | Tetratricopeptide repeat-containing protein. | Fe-S protein assembly chaperone; Belongs to the heat shock protein 70 family. | 0.728 |
| FAD_0607 | dnaJ | FAD_0607 | FAD_0534 | Pentatricopeptide repeat-containing protein. | Chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and [...] | 0.714 |
| FAD_0607 | dnaK | FAD_0607 | FAD_0533 | Pentatricopeptide repeat-containing protein. | Chaperone DnaK; Acts as a chaperone. | 0.728 |
| FAD_0607 | hscA | FAD_0607 | FAD_0761 | Pentatricopeptide repeat-containing protein. | Fe-S protein assembly chaperone; Belongs to the heat shock protein 70 family. | 0.728 |
| FAD_0956 | dnaJ | FAD_0956 | FAD_0534 | Tetratricopeptide repeat-containing protein. | Chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and [...] | 0.749 |
| FAD_0956 | dnaK | FAD_0956 | FAD_0533 | Tetratricopeptide repeat-containing protein. | Chaperone DnaK; Acts as a chaperone. | 0.728 |
| FAD_0956 | hscA | FAD_0956 | FAD_0761 | Tetratricopeptide repeat-containing protein. | Fe-S protein assembly chaperone; Belongs to the heat shock protein 70 family. | 0.728 |
| FAD_1190 | dnaJ | FAD_1190 | FAD_0534 | Tetratricopeptide repeat-containing protein. | Chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and [...] | 0.714 |
| FAD_1190 | dnaK | FAD_1190 | FAD_0533 | Tetratricopeptide repeat-containing protein. | Chaperone DnaK; Acts as a chaperone. | 0.728 |
| FAD_1190 | hscA | FAD_1190 | FAD_0761 | Tetratricopeptide repeat-containing protein. | Fe-S protein assembly chaperone; Belongs to the heat shock protein 70 family. | 0.728 |
| FAD_1468 | FAD_1525 | FAD_1468 | FAD_1525 | Thermosome subunit; Belongs to the TCP-1 chaperonin family. | Thermosome subunit; Belongs to the TCP-1 chaperonin family. | 0.999 |
| FAD_1468 | dnaJ | FAD_1468 | FAD_0534 | Thermosome subunit; Belongs to the TCP-1 chaperonin family. | Chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and [...] | 0.799 |
| FAD_1468 | dnaK | FAD_1468 | FAD_0533 | Thermosome subunit; Belongs to the TCP-1 chaperonin family. | Chaperone DnaK; Acts as a chaperone. | 0.842 |
| FAD_1468 | grpE | FAD_1468 | FAD_0532 | Thermosome subunit; Belongs to the TCP-1 chaperonin family. | Chaperone GrpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent [...] | 0.927 |
| FAD_1468 | hscA | FAD_1468 | FAD_0761 | Thermosome subunit; Belongs to the TCP-1 chaperonin family. | Fe-S protein assembly chaperone; Belongs to the heat shock protein 70 family. | 0.842 |
| FAD_1468 | rpl10e | FAD_1468 | FAD_0226 | Thermosome subunit; Belongs to the TCP-1 chaperonin family. | 50S ribosomal protein L10e; Belongs to the universal ribosomal protein uL16 family. | 0.527 |
| FAD_1525 | FAD_1468 | FAD_1525 | FAD_1468 | Thermosome subunit; Belongs to the TCP-1 chaperonin family. | Thermosome subunit; Belongs to the TCP-1 chaperonin family. | 0.999 |
| FAD_1525 | dnaJ | FAD_1525 | FAD_0534 | Thermosome subunit; Belongs to the TCP-1 chaperonin family. | Chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and [...] | 0.799 |
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